title: [Ethanol-metabolizing enzymes from human testis].
abstract: Testicular ethanol-metabolizing enzymes (alcohol dehydrogenase, microsomal ethanol-oxidizing system, catalase) were investigated. Alcohol dehydrogenase was purified to homogeneity and its main kinetic parameters were analyzed. It was shown that alcohol dehydrogenase corresponds to class III isozymes and does not participate in ethanol oxidation. The testicular microsomal ethanol-oxidizing activity does not exceed 0.02 nmol/min/mg of protein. The activity of catalase and its peroxidase component is far lower in the testes than in the liver. On the whole, testicular tissue is rather inactive in respect of ethanol oxidation.
authors.forename: P P
authors.initials: PP
authors.lastname: Voronov
authors.forename: A M
authors.initials: AM
authors.lastname: Khokha
mesh_terms: D000426:Alcohol Dehydrogenase / Q000302:isolation & purification* / Q000378:metabolism; D002374:Catalase / Q000302:isolation & purification* / Q000378:metabolism; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D000431:Ethanol / Q000378:metabolism*; D006801:Humans; D007527:Isoenzymes / Q000302:isolation & purification / Q000378:metabolism; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D008297:Male; D008861:Microsomes / Q000201:enzymology; D013737:Testis / Q000201:enzymology*
chemical_list: D007527:Isoenzymes; D000431:Ethanol; D000426:Alcohol Dehydrogenase; D002374:Catalase
vernacular_title: Etanolmetaboliziruiushchie fermenty semennikov cheloveka.